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Open AccessJournal ArticleDOI

Protein folding at single-molecule resolution.

Allan Chris M. Ferreon, +1 more
- 01 Aug 2011 - 
- Vol. 1814, Iss: 8, pp 1021-1029
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TLDR
This review briefly introduces common FRET and force methods, and then explores several areas of protein folding where single-molecule experiments have yielded insights, including exciting new information about folding landscapes, dynamics, intermediates, unfolded ensembles, intrinsically disordered proteins, assisted folding and biomechanical unfolding.
About
This article is published in Biochimica et Biophysica Acta.The article was published on 2011-08-01 and is currently open access. It has received 53 citations till now. The article focuses on the topics: Intrinsically disordered proteins & Protein folding.

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Citations
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Journal ArticleDOI

Mechanical properties of viruses analyzed by atomic force microscopy: A virological perspective

TL;DR: The perspective of structural and molecular virology is adopted to review the results obtained to date, using the atomic force microscope, on the mechanical properties of virus particles, their molecular determinants, and possible biological implications.

Detecting the Conformation of Individual Proteins in Live Cells using Single Molecule Fluorescence Resonance Energy Transfer

John J. Sakon
TL;DR: Single-molecule fluorescence resonance energy transfer with single-particle tracking in live cells to detect the in vivo conformation of individual proteins shows the potential of this method to reveal dynamic interactions within cells.
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Disentangling Subpopulations in Single-Molecule FRET and ALEX Experiments with Photon Distribution Analysis

TL;DR: This work determines the FRET efficiency and brightness ratio distributions and uses them to reveal the underlying structure of a two-state DNA-hairpin and a DNA hairpin that is bound to DNA origami, and uses it to identify and isolate static and dynamic subpopulations.
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Intrinsically Disordered Proteins: From Sequence and Conformational Properties toward Drug Discovery

TL;DR: Progress in the experimental characterization of IDPs has been made in the last decade, especially in NMR spectroscopy and small‐angle X‐ray scattering as well as in single‐molecule techniques, and these advances have paved the way to targeting IDP interactions in rational drug‐discovery projects.
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Computational Amide I 2D IR Spectroscopy as a Probe of Protein Structure and Dynamics

TL;DR: Two-dimensional infrared spectroscopy of amide I vibrations is increasingly being used to study the structure and dynamics of proteins and peptides, and quantitative modeling of time-dependent structural ensembles and of direct feedback between experiments and simulations is possible.
References
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Journal ArticleDOI

Living with water stress: evolution of osmolyte systems

TL;DR: Osmolyte compatibility is proposed to result from the absence of osmolytes interactions with substrates and cofactors, and the nonperturbing or favorable effects of oSMolytes on macromolecular-solvent interactions.
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Reversible Unfolding of Individual Titin Immunoglobulin Domains by AFM

TL;DR: Single-molecule atomic force microscopy was used to investigate the mechanical properties of titin, the giant sarcomeric protein of striated muscle, and refolding of immunoglobulin domains was observed.
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The energy landscapes and motions of proteins.

TL;DR: The concepts that emerge from studies of the conformational substates and the motions between them permit a quantitative discussion of one simple reaction, the binding of small ligands such as carbon monoxide to myoglobin.
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Entropy production fluctuation theorem and the nonequilibrium work relation for free energy differences

TL;DR: A generalized version of the fluctuation theorem is derived for stochastic, microscopically reversible dynamics and this generalized theorem provides a succinct proof of the nonequilibrium work relation.
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Intrinsically unstructured proteins.

TL;DR: In this review, recent findings are surveyed to illustrate that this novel but rapidly advancing field has reached a point where proteins can be comprehensively classified on the basis of structure and function.
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